Purification and characterization of a β-1,4-glucosidase from a newly isolated strain of Fomitopsis pinicola

摘要: An efficient s-1,4-glucosidase (BGL) producing strain, Fomitopsis pinicola KMJ812, was isolated and identified based on morphological features sequence analysis of internal transcribed spacer rDNA. extracellular BGL purified to homogeneity by sequential chromatography F. culture supernatants a DEAE-sepharose column, gel filtration then Mono Q column with fast protein liquid chromatography. The relative molecular weight determined be 105 kDa sodium dodecylsulfate-polyacrylamide electrophoresis, or 110 kDa size exclusion chromatography, indicating that the enzyme is monomer. hydrolytic activity had pH optimum 4.5 temperature 50°C. showed high substrate specificity catalytic efficiency (k cat = 2,990 s−1, K m = 1.76 mM, k cat/K m = 1,700 mM−1 s−1) for p-nitrophenyl-β-d-glucopyranoside. Its amino acid sequences significant homology hydrolases from glycoside hydrolase family 3, member 3. Although BGLs have been characterized several other sources, distinguished its strict specificity.